Detail Information for IndEnz0002004068
IED ID IndEnz0002004068
Enzyme Type ID protease004068
Protein Name Ferrochelatase, mitochondrial
EC 4.99.1.1
Heme synthase
Protoheme ferro-lyase
Gene Name HEM15 YOR176W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MLSRTIRTQGSFLRRSQLTITRSFSVTFNMQNAQKRSPTGIVLMNMGGPSKVEETYDFLYQLFADNDLIPISAKYQKTIAKYIAKFRTPKIEKQYREIGGGSPIRKWSEYQATEVCKILDKTCPETAPHKPYVAFRYAKPLTAETYKQMLKDGVKKAVAFSQYPHFSYSTTGSSINELWRQIKALDSERSISWSVIDRWPTNEGLIKAFSENITKKLQEFPQPVRDKVVLLFSAHSLPMDVVNTGDAYPAEVAATVYNIMQKLKFKNPYRLVWQSQVGPKPWLGAQTAEIAEFLGPKVDGLMFIPIAFTSDHIETLHEIDLGVIGESEYKDKFKRCESLNGNQTFIEGMADLVKSHLQSNQLYSNQLPLDFALGKSNDPVKDLSLVFGNHEST
Enzyme Length 393
Uniprot Accession Number P16622
Absorption
Active Site ACT_SITE 351; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX; Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
DNA Binding
EC Number 4.99.1.1
Enzyme Function FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
nucleotide Binding
Features Active site (1); Beta strand (12); Chain (1); Helix (19); Sequence conflict (1); Transit peptide (1); Turn (4)
Keywords 3D-structure;Direct protein sequencing;Heme biosynthesis;Iron;Lyase;Membrane;Mitochondrion;Mitochondrion inner membrane;Porphyrin biosynthesis;Reference proteome;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Note=It is bound to the mitochondrial inner membrane in eukaryotic cells with its active site on the matrix side of the membrane.
Modified Residue
Post Translational Modification PTM: The leader peptide may be processed in two proteolytic steps, first between Ser-23 and Phe-24, second and by a different protease, to yield the mature protein.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1L8X; 1LBQ;
Mapped Pubmed ID 10858295; 11212295; 11283351; 11805837; 11831847; 11939775; 12427010; 12668611; 1304908; 16697062; 16843540; 17352532; 18156292; 18227070; 18593702; 18779372; 19930686; 20008079; 21776189; 24130505; 25028499; 25640729; 25999509; 26354769; 27026703; 27317660; 27387517; 7035824; 7629135; 8473299; 8818224;
Motif
Gene Encoded By
Mass 44,596
Kinetics
Metal Binding
Rhea ID RHEA:22584
Cross Reference Brenda 4.99.1.1;